کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2050707 1074178 2008 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
The second von Willebrand type A domain of cochlin has high affinity for type I, type II and type IV collagens
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
The second von Willebrand type A domain of cochlin has high affinity for type I, type II and type IV collagens
چکیده انگلیسی

Cochlin is colocalized with type II collagen in the extracellular matrix of cochlea and has been suggested to interact with this collagen. Here we show that the second von Willebrand type A domain of cochlin has affinity for type II collagen, as well as type I and type IV collagens whereas the LCCL-domain of cochlin has no affinity for these proteins. The implications of these findings for the mechanism whereby cochlin mutations cause the dominant negative DFNA9-type hearing loss are discussed.Structured summaryMINT-6796048:type I collagen (uniprotkb:P02452) binds (MI:0407) to cochlin-vWA2 uniprotkb:O43405) by surface plasmon resonance (MI:0107)MINT-6796166:type III collagen (uniprotkb:P02462) binds (MI:0407) to cochlin-vWA2 (uniprotkb:O43405) by surface plasmon resonance (MI:0107)MINT-6796062:type II collagen (uniprotkb:P02458) binds (MI:0407) to cochlin-vWA2 (uniprotkb:O43405) by surface plasmon resonance (MI:0107)

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 582, Issue 29, 10 December 2008, Pages 4003–4007
نویسندگان
, , ,